Binding surfaces are used in a wide variety of applications including, for example, affinity assays. Conventional binding surfaces are typically prepared by maximizing the amount of ligand binders per unit surface area of the solid phase support surface. Although the conventional approach results in a support surface with a high density of ligand binders, simply maximizing the number of ligand binders on a support surface does not invariably improve performance of the binding surface. Some conventional binding surfaces used in affinity assays maximize binding capacity by direct coating of a ligand binder such as an antibody, or a biotin-specific ligand binder such as SA, onto a solid phase and blocking the solid phase with bovine serum albumin (BSA) or ovalbumin. Although this maximizes the antigen or biotin binding capacity of the binding surface, the respective antibodies or biotin-specific ligand binders are crowded on the binding surface without specific orientation, and traditional blocking strategies do not necessarily prevent or mitigate sloughing of antibodies or biotin-specific ligand binders from the binding surface. Further, sloughing can result in poor assay sensitivity (sub-optimal signal-to-noise ratio), accuracy, precision, stability, or manufacturability, or combinations thereof. Binding surface crowding and random orientation can decrease binding efficiency or capacity of the binding surface due to steric hindrance. Accordingly, there is a need for improved binding surfaces and compositions and methods for making improved binding surfaces that do not rely on simply maximizing the density of ligand binders on a binding surface.